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P19784

- CSK22_HUMAN

UniProt

P19784 - CSK22_HUMAN

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Protein

Casein kinase II subunit alpha'

Gene

CSNK2A2

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli

Functioni

Catalytic subunit of a constitutively active serine/threonine-protein kinase complex that phosphorylates a large number of substrates containing acidic residues C-terminal to the phosphorylated serine or threonine. Regulates numerous cellular processes, such as cell cycle progression, apoptosis and transcription, as well as viral infection. May act as a regulatory node which integrates and coordinates numerous signals leading to an appropriate cellular response. During mitosis, functions as a component of the p53/TP53-dependent spindle assembly checkpoint (SAC) that maintains cyclin-B-CDK1 activity and G2 arrest in response to spindle damage. Also required for p53/TP53-mediated apoptosis, phosphorylating 'Ser-392' of p53/TP53 following UV irradiation. Can also negatively regulate apoptosis. Phosphorylates the caspases CASP9 and CASP2 and the apoptotic regulator NOL3. Phosphorylation protects CASP9 from cleavage and activation by CASP8, and inhibits the dimerization of CASP2 and activation of CASP8. Regulates transcription by direct phosphorylation of RNA polymerases I, II, III and IV. Also phosphorylates and regulates numerous transcription factors including NF-kappa-B, STAT1, CREB1, IRF1, IRF2, ATF1, SRF, MAX, JUN, FOS, MYC and MYB. Phosphorylates Hsp90 and its co-chaperones FKBP4 and CDC37, which is essential for chaperone function. Regulates Wnt signaling by phosphorylating CTNNB1 and the transcription factor LEF1. Acts as an ectokinase that phosphorylates several extracellular proteins. During viral infection, phosphorylates various proteins involved in the viral life cycles of EBV, HSV, HBV, HCV, HIV, CMV and HPV.3 Publications

Catalytic activityi

ATP + a protein = ADP + a phosphoprotein.

Enzyme regulationi

Constitutively active protein kinase whose activity is not directly affected by phosphorylation. Seems to be regulated by level of expression and localization (By similarity).By similarity

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei69 – 691ATPPROSITE-ProRule annotation
Active sitei157 – 1571Proton acceptorPROSITE-ProRule annotation

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi46 – 549ATPPROSITE-ProRule annotation

GO - Molecular functioni

  1. ATP binding Source: UniProtKB-KW
  2. protein N-terminus binding Source: UniProtKB
  3. protein serine/threonine kinase activity Source: UniProtKB-KW

GO - Biological processi

  1. apoptotic process Source: UniProtKB-KW
  2. axon guidance Source: Reactome
  3. mitotic cell cycle Source: Reactome
  4. mitotic spindle checkpoint Source: UniProtKB
  5. regulation of transcription, DNA-templated Source: UniProtKB-KW
  6. transcription, DNA-templated Source: UniProtKB-KW
  7. Wnt signaling pathway Source: UniProtKB-KW
Complete GO annotation...

Keywords - Molecular functioni

Kinase, Serine/threonine-protein kinase, Transferase

Keywords - Biological processi

Apoptosis, Cell cycle, Transcription, Transcription regulation, Wnt signaling pathway

Keywords - Ligandi

ATP-binding, Nucleotide-binding

Enzyme and pathway databases

BRENDAi2.7.11.1. 2681.
ReactomeiREACT_150260. Condensation of Prometaphase Chromosomes.
REACT_200668. WNT mediated activation of DVL.
REACT_22272. Signal transduction by L1.
SignaLinkiP19784.

Names & Taxonomyi

Protein namesi
Recommended name:
Casein kinase II subunit alpha' (EC:2.7.11.1)
Short name:
CK II alpha'
Gene namesi
Name:CSNK2A2
Synonyms:CK2A2
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 16

Organism-specific databases

HGNCiHGNC:2459. CSNK2A2.

Subcellular locationi

GO - Cellular componenti

  1. cytosol Source: Reactome
  2. nucleus Source: UniProtKB
Complete GO annotation...

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA26959.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 350350Casein kinase II subunit alpha'PRO_0000085891Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei13 – 131Phosphotyrosine1 Publication
Modified residuei18 – 181Phosphoserine2 Publications
Modified residuei21 – 211Phosphoserine2 Publications
Modified residuei97 – 971N6-acetyllysine1 Publication
Modified residuei288 – 2881Phosphoserine2 Publications

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

MaxQBiP19784.
PaxDbiP19784.
PeptideAtlasiP19784.
PRIDEiP19784.

2D gel databases

SWISS-2DPAGEP19784.

PTM databases

PhosphoSiteiP19784.

Expressioni

Gene expression databases

BgeeiP19784.
CleanExiHS_CSNK2A2.
ExpressionAtlasiP19784. baseline and differential.
GenevestigatoriP19784.

Interactioni

Subunit structurei

Heterotetramer composed of two catalytic subunits (alpha chain and/or alpha' chain) and two regulatory subunits (beta chains). The tetramer can exist as a combination of 2 alpha/2 beta, 2 alpha'/2 beta or 1 alpha/1 alpha'/2 beta subunits. Also part of a CK2-SPT16-SSRP1 complex composed of SSRP1, SUPT16H, CSNK2A1, CSNK2A2 and CSNK2B, which forms following UV irradiation. Interacts with RNPS1.3 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
CSNK2A1P684003EBI-347451,EBI-347804
CSNK2BP678706EBI-347451,EBI-348169
KIF5CO602824EBI-347451,EBI-717170

Protein-protein interaction databases

BioGridi107842. 144 interactions.
DIPiDIP-318N.
IntActiP19784. 93 interactions.
MINTiMINT-5004107.
STRINGi9606.ENSP00000262506.

Structurei

Secondary structure

1
350
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi11 – 133
Turni14 – 163
Helixi17 – 193
Helixi22 – 254
Helixi27 – 293
Helixi37 – 393
Beta strandi40 – 489
Beta strandi50 – 5910
Turni60 – 634
Beta strandi64 – 718
Helixi76 – 8813
Turni89 – 913
Beta strandi98 – 1036
Turni105 – 1073
Beta strandi110 – 1156
Helixi122 – 1254
Helixi131 – 15020
Helixi160 – 1623
Beta strandi163 – 1664
Turni167 – 1704
Beta strandi171 – 1744
Helixi196 – 1983
Helixi201 – 2044
Helixi213 – 22816
Beta strandi231 – 2344
Helixi239 – 25012
Helixi252 – 26110
Helixi270 – 2734
Helixi282 – 2854
Turni288 – 2903
Helixi291 – 2933
Helixi296 – 30510
Turni310 – 3123
Helixi316 – 3205
Helixi323 – 3253
Helixi326 – 3316

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
3E3BX-ray3.20X1-334[»]
3OFMX-ray2.00A1-350[»]
3U87X-ray2.90A/B327-350[»]
ProteinModelPortaliP19784.
SMRiP19784. Positions 8-332.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP19784.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini40 – 325286Protein kinasePROSITE-ProRule annotationAdd
BLAST

Sequence similaritiesi

Belongs to the protein kinase superfamily. Ser/Thr protein kinase family. CK2 subfamily.PROSITE-ProRule annotation
Contains 1 protein kinase domain.PROSITE-ProRule annotation

Phylogenomic databases

eggNOGiCOG0515.
GeneTreeiENSGT00390000004215.
HOGENOMiHOG000233021.
HOVERGENiHBG107282.
KOiK03097.
OMAiPSWGNQD.
OrthoDBiEOG7QG446.
PhylomeDBiP19784.
TreeFamiTF300483.

Family and domain databases

InterProiIPR011009. Kinase-like_dom.
IPR000719. Prot_kinase_dom.
IPR017441. Protein_kinase_ATP_BS.
IPR002290. Ser/Thr_dual-sp_kinase.
IPR008271. Ser/Thr_kinase_AS.
[Graphical view]
PfamiPF00069. Pkinase. 1 hit.
[Graphical view]
SMARTiSM00220. S_TKc. 1 hit.
[Graphical view]
SUPFAMiSSF56112. SSF56112. 1 hit.
PROSITEiPS00107. PROTEIN_KINASE_ATP. 1 hit.
PS50011. PROTEIN_KINASE_DOM. 1 hit.
PS00108. PROTEIN_KINASE_ST. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

P19784-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MPGPAAGSRA RVYAEVNSLR SREYWDYEAH VPSWGNQDDY QLVRKLGRGK
60 70 80 90 100
YSEVFEAINI TNNERVVVKI LKPVKKKKIK REVKILENLR GGTNIIKLID
110 120 130 140 150
TVKDPVSKTP ALVFEYINNT DFKQLYQILT DFDIRFYMYE LLKALDYCHS
160 170 180 190 200
KGIMHRDVKP HNVMIDHQQK KLRLIDWGLA EFYHPAQEYN VRVASRYFKG
210 220 230 240 250
PELLVDYQMY DYSLDMWSLG CMLASMIFRR EPFFHGQDNY DQLVRIAKVL
260 270 280 290 300
GTEELYGYLK KYHIDLDPHF NDILGQHSRK RWENFIHSEN RHLVSPEALD
310 320 330 340 350
LLDKLLRYDH QQRLTAKEAM EHPYFYPVVK EQSQPCADNA VLSSGLTAAR
Length:350
Mass (Da):41,213
Last modified:February 1, 1991 - v1
Checksum:i3ECB92F6BD3DD7F1
GO

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti188 – 1881E → A.1 Publication
Corresponds to variant rs55911801 [ dbSNP | Ensembl ].
VAR_040416

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
M55268 mRNA. Translation: AAA51548.1.
BC008812 mRNA. Translation: AAH08812.1.
CCDSiCCDS10794.1.
PIRiB35838.
RefSeqiNP_001887.1. NM_001896.2.
UniGeneiHs.82201.

Genome annotation databases

EnsembliENST00000262506; ENSP00000262506; ENSG00000070770.
GeneIDi1459.
KEGGihsa:1459.
UCSCiuc002enc.3. human.

Polymorphism databases

DMDMi125266.

Keywords - Coding sequence diversityi

Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
M55268 mRNA. Translation: AAA51548.1 .
BC008812 mRNA. Translation: AAH08812.1 .
CCDSi CCDS10794.1.
PIRi B35838.
RefSeqi NP_001887.1. NM_001896.2.
UniGenei Hs.82201.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
3E3B X-ray 3.20 X 1-334 [» ]
3OFM X-ray 2.00 A 1-350 [» ]
3U87 X-ray 2.90 A/B 327-350 [» ]
ProteinModelPortali P19784.
SMRi P19784. Positions 8-332.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 107842. 144 interactions.
DIPi DIP-318N.
IntActi P19784. 93 interactions.
MINTi MINT-5004107.
STRINGi 9606.ENSP00000262506.

Chemistry

BindingDBi P19784.
ChEMBLi CHEMBL4070.
GuidetoPHARMACOLOGYi 1550.

PTM databases

PhosphoSitei P19784.

Polymorphism databases

DMDMi 125266.

2D gel databases

SWISS-2DPAGE P19784.

Proteomic databases

MaxQBi P19784.
PaxDbi P19784.
PeptideAtlasi P19784.
PRIDEi P19784.

Protocols and materials databases

DNASUi 1459.
Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000262506 ; ENSP00000262506 ; ENSG00000070770 .
GeneIDi 1459.
KEGGi hsa:1459.
UCSCi uc002enc.3. human.

Organism-specific databases

CTDi 1459.
GeneCardsi GC16M058191.
HGNCi HGNC:2459. CSNK2A2.
MIMi 115442. gene.
neXtProti NX_P19784.
PharmGKBi PA26959.
GenAtlasi Search...

Phylogenomic databases

eggNOGi COG0515.
GeneTreei ENSGT00390000004215.
HOGENOMi HOG000233021.
HOVERGENi HBG107282.
KOi K03097.
OMAi PSWGNQD.
OrthoDBi EOG7QG446.
PhylomeDBi P19784.
TreeFami TF300483.

Enzyme and pathway databases

BRENDAi 2.7.11.1. 2681.
Reactomei REACT_150260. Condensation of Prometaphase Chromosomes.
REACT_200668. WNT mediated activation of DVL.
REACT_22272. Signal transduction by L1.
SignaLinki P19784.

Miscellaneous databases

ChiTaRSi CSNK2A2. human.
EvolutionaryTracei P19784.
GeneWikii CSNK2A2.
GenomeRNAii 1459.
NextBioi 5997.
PROi P19784.
SOURCEi Search...

Gene expression databases

Bgeei P19784.
CleanExi HS_CSNK2A2.
ExpressionAtlasi P19784. baseline and differential.
Genevestigatori P19784.

Family and domain databases

InterProi IPR011009. Kinase-like_dom.
IPR000719. Prot_kinase_dom.
IPR017441. Protein_kinase_ATP_BS.
IPR002290. Ser/Thr_dual-sp_kinase.
IPR008271. Ser/Thr_kinase_AS.
[Graphical view ]
Pfami PF00069. Pkinase. 1 hit.
[Graphical view ]
SMARTi SM00220. S_TKc. 1 hit.
[Graphical view ]
SUPFAMi SSF56112. SSF56112. 1 hit.
PROSITEi PS00107. PROTEIN_KINASE_ATP. 1 hit.
PS50011. PROTEIN_KINASE_DOM. 1 hit.
PS00108. PROTEIN_KINASE_ST. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. "Isolation and characterization of human cDNA clones encoding the alpha and the alpha' subunits of casein kinase II."
    Lozeman F.J., Litchfield D.W., Piening C., Takio K., Walsh K.A., Krebs E.G.
    Biochemistry 29:8436-8447(1990) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
  2. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
    The MGC Project Team
    Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Tissue: Ovary.
  3. "A DNA damage-induced p53 serine 392 kinase complex contains CK2, hSpt16, and SSRP1."
    Keller D.M., Zeng X., Wang Y., Zhang Q.H., Kapoor M., Shu H., Goodman R., Lozano G., Zhao Y., Lu H.
    Mol. Cell 7:283-292(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, INTERACTION WITH SSRP1 AND SUPT16H.
  4. "Protein kinase CK2 is involved in G2 arrest and apoptosis following spindle damage in epithelial cells."
    Sayed M., Pelech S., Wong C., Marotta A., Salh B.
    Oncogene 20:6994-7005(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION IN CELL CYCLE.
  5. "p53 serine 392 phosphorylation increases after UV through induction of the assembly of the CK2.hSPT16.SSRP1 complex."
    Keller D.M., Lu H.
    J. Biol. Chem. 277:50206-50213(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH SSRP1 AND SUPT16H.
  6. "Caspase-2 primes cancer cells for TRAIL-mediated apoptosis by processing procaspase-8."
    Shin S., Lee Y., Kim W., Ko H., Choi H., Kim K.
    EMBO J. 24:3532-3542(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION IN APOPTOSIS.
  7. "One-thousand-and-one substrates of protein kinase CK2?"
    Meggio F., Pinna L.A.
    FASEB J. 17:349-368(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: REVIEW ON FUNCTION.
  8. "Kinase-selective enrichment enables quantitative phosphoproteomics of the kinome across the cell cycle."
    Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R., Greff Z., Keri G., Stemmann O., Mann M.
    Mol. Cell 31:438-448(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-18; SER-21 AND SER-288, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  9. "Protein kinase CK2 in health and disease: Protein kinase CK2: from structures to insights."
    Niefind K., Raaf J., Issinger O.G.
    Cell. Mol. Life Sci. 66:1800-1816(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: REVIEW ON STRUCTURE.
  10. "Protein kinase CK2 in health and disease: From birth to death: the role of protein kinase CK2 in the regulation of cell proliferation and survival."
    St-Denis N.A., Litchfield D.W.
    Cell. Mol. Life Sci. 66:1817-1829(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: REVIEW ON FUNCTION.
  11. "Protein kinase CK2 in health and disease: Cellular functions of protein kinase CK2: a dynamic affair."
    Filhol O., Cochet C.
    Cell. Mol. Life Sci. 66:1830-1839(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: REVIEW ON FUNCTION.
  12. "Protein kinase CK2 in health and disease: CK2: the kinase controlling the Hsp90 chaperone machinery."
    Miyata Y.
    Cell. Mol. Life Sci. 66:1840-1849(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: REVIEW ON FUNCTION IN REGULATION OF HSP90.
  13. "Protein kinase CK2 in health and disease: CK2 and its role in Wnt and NF-kappaB signaling: linking development and cancer."
    Dominguez I., Sonenshein G.E., Seldin D.C.
    Cell. Mol. Life Sci. 66:1850-1857(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: REVIEW ON FUNCTION IN WNT SIGNALING.
  14. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-13; SER-18; SER-21 AND SER-288, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  15. "Lysine acetylation targets protein complexes and co-regulates major cellular functions."
    Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.C., Olsen J.V., Mann M.
    Science 325:834-840(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-97, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  16. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  17. "Structure of human protein kinase CK2 alpha 2 with a potent indazole-derivative inhibitor."
    Nakaniwa T., Kinoshita T., Sekiguchi Y., Tada T., Nakanishi I., Kitaura K., Suzuki Y., Ohno H., Hirasawa A., Tsujimoto G.
    Acta Crystallogr. F 65:75-79(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (3.20 ANGSTROMS) OF 1-334 IN COMPLEX WITH INHIBITOR.
  18. "Structure of the human protein kinase CK2 catalytic subunit CK2alpha' and interaction thermodynamics with the regulatory subunit CK2beta."
    Bischoff N., Olsen B., Raaf J., Bretner M., Issinger O.G., Niefind K.
    J. Mol. Biol. 407:1-12(2011) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.00 ANGSTROMS).
  19. "Patterns of somatic mutation in human cancer genomes."
    Greenman C., Stephens P., Smith R., Dalgliesh G.L., Hunter C., Bignell G., Davies H., Teague J., Butler A., Stevens C., Edkins S., O'Meara S., Vastrik I., Schmidt E.E., Avis T., Barthorpe S., Bhamra G., Buck G.
    , Choudhury B., Clements J., Cole J., Dicks E., Forbes S., Gray K., Halliday K., Harrison R., Hills K., Hinton J., Jenkinson A., Jones D., Menzies A., Mironenko T., Perry J., Raine K., Richardson D., Shepherd R., Small A., Tofts C., Varian J., Webb T., West S., Widaa S., Yates A., Cahill D.P., Louis D.N., Goldstraw P., Nicholson A.G., Brasseur F., Looijenga L., Weber B.L., Chiew Y.-E., DeFazio A., Greaves M.F., Green A.R., Campbell P., Birney E., Easton D.F., Chenevix-Trench G., Tan M.-H., Khoo S.K., Teh B.T., Yuen S.T., Leung S.Y., Wooster R., Futreal P.A., Stratton M.R.
    Nature 446:153-158(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: VARIANT [LARGE SCALE ANALYSIS] ALA-188.

Entry informationi

Entry nameiCSK22_HUMAN
AccessioniPrimary (citable) accession number: P19784
Entry historyi
Integrated into UniProtKB/Swiss-Prot: February 1, 1991
Last sequence update: February 1, 1991
Last modified: October 29, 2014
This is version 156 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Miscellaneousi

Miscellaneous

Can use both ATP and GTP as phosphoryl donors. Phosphorylation by casein kinase 2 has been estimated to represent up to one quarter of the eukaryotic phosphoproteome.

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. Human chromosome 16
    Human chromosome 16: entries, gene names and cross-references to MIM
  2. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  3. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  4. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  5. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  6. Human and mouse protein kinases
    Human and mouse protein kinases: classification and index
  7. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3